trans-2-Phenylcyclopropylamine is a substrate for and inactivator of horseradish peroxidase
- 5 September 1996
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1296 (2) , 250-256
- https://doi.org/10.1016/0167-4838(96)00084-2
Abstract
No abstract availableKeywords
Funding Information
- National Science Foundation (CHE 87-06263, GM 48812)
- National Institutes of Health (NS 22688)
This publication has 21 references indexed in Scilit:
- Molecular Engineering of Horseradish Peroxidase: Thioether Sulfoxidation and Styrene Epoxidation by Phe-41 Leucine and Threonine MutantsJournal of the American Chemical Society, 1995
- 2D NMR Approaches to Characterizing the Molecular Structure and Dynamic Stability of the Active Site for Cyanide-Inhibited Horseradish PeroxidaseJournal of the American Chemical Society, 1994
- The oxidation of 4-aminobiphenyl by horseradish peroxidaseChemical Research in Toxicology, 1992
- 3-aminotriazole is a substrate for lactoperoxidase but not for catalaseBiochemical and Biophysical Research Communications, 1991
- Peroxygenation mechanism for chloroperoxidase-catalyzed N-oxidation of arylaminesChemical Research in Toxicology, 1991
- Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agentBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Differences in the binding of aromatic substrates to horseradish peroxidase revealed by fluorescence line narrowingBiochemistry, 1989
- In vitro metabolic transformations of vinblastine: oxidations catalyzed by peroxidaseJournal of Medicinal Chemistry, 1989
- Studies on the ethylhydroperoxide-supported oxidation of 1,4-diazabicyclo(2.2.2)octane by chloroperoxidase.CHEMICAL & PHARMACEUTICAL BULLETIN, 1988
- One-Electron Oxidation of Vindoline and 16-O-Acetylvindoline Catalyzed by PeroxidaseJournal of Medicinal Chemistry, 1985